EF2_METKA
ID EF2_METKA Reviewed; 1257 AA.
AC Q8TXJ4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Elongation factor 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Contains:
DE RecName: Full=Mka FusA intein;
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=MK0679;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome. {ECO:0000255|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000250}.
CC -!- MISCELLANEOUS: The intein interrupts the GTP-binding site.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00054}.
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DR EMBL; AE009439; AAM01894.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TXJ4; -.
DR SMR; Q8TXJ4; -.
DR STRING; 190192.MK0679; -.
DR EnsemblBacteria; AAM01894; AAM01894; MK0679.
DR KEGG; mka:MK0679; -.
DR PATRIC; fig|190192.8.peg.718; -.
DR HOGENOM; CLU_265167_0_0_2; -.
DR OMA; IEWISHE; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.28.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_A; EF_G_EF_2_A; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004543; Transl_elong_EFG/EF2_arc.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR00490; aEF-2; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Cytoplasm; Elongation factor; Endonuclease;
KW GTP-binding; Hydrolase; Intron homing; Nuclease; Nucleotide-binding;
KW Protein biosynthesis; Protein splicing; Reference proteome.
FT CHAIN 1..34
FT /note="Elongation factor 2, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007436"
FT CHAIN 35..556
FT /note="Mka FusA intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007437"
FT CHAIN 557..1257
FT /note="Elongation factor 2, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007438"
FT DOMAIN 273..402
FT /note="DOD-type homing endonuclease"
FT DOMAIN 541..782
FT /note="tr-type G"
FT REGION 1237..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 616..620
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 670..673
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT MOD_RES 1120
FT /note="Diphthamide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 1257 AA; 142071 MW; 2C916583EF9D9B3C CRC64;
MGRKEKMAEK CRKLMTEPGK IRNIGIIAHI DHGKCVAPET KICLADGRFV RADELFEELK
ERGRLVKCDE SEEVYELREP VGVSSLDKDA VEIVEGKITH VWRLKADKLV EVEVKNGRSI
RTTPEHKFLV LDPSGEIVEK RADELEIGDY IVCTQKLVHE GMSEEELKRE VFRRLGRDFF
VHLPEEEAES VLELAKERGI KALWETLEVD IEENSFYYQL RKGRIRADIL VDLAEELGLD
LADLYDAVEV SYRSNTKSTK PIRLPEPEDL FYLAGLMFGD GCWNQLTNGS EAIQGEVKRI
ASDMGLEVRV RRYEGKTARI DFPETVPRIL EALFDYPRRK KAHRIRVNDF LTRAPLDCIA
EFIRGYFDAD GTVEEGRSAV SVTSVSREFL EDLQLLLQKF DVASYLREGD GAYTLYVSGA
RSLERFPGFR EPEKAEKLKK LMEKASSSEL EKVPISGEIL REVRGDVPTT RMFNCYSNYE
GGQVGLTKSS LEKVISTLEA VGVEGEALER LKALARDDVC FLEVVRVEEV EYDGYVYDFT
VEEHHNFAAE GFVVHNTTLS DQLLAGAGMI SEELAGDQLV LDFDEMEQER GITIDAANVS
MVHEYEGEEY LINLIDTPGH VDFSGDVTRA MRAVDGAIVV VCAVEGVMPQ TETVLRQALR
ERVRPVLYIN KVDRLINELK LSPEEMQNRF LEIISEVNKM IEQMAPEEFK DEWKVSVEDG
SVAFGSAYYG WGISFPFMEK TGITFKDIIE YCQQDKQKEL AQEAPVYQVV LDMVVKHLPD
PVTAQEYRIE QIWPGDPESE DGKTLRKCDP NGKLAMVVTD VRIDEHAGEV ATGRVYSGTI
REGQQVYLAS SKKETRVQQV GIYMGPDRIR TDEVPAGNIA AVTGLRDVWA GETVTDPEDP
IEPFEELQHF AEPVVTVAVE AKNTQDLPKL IEILHQIAKE DPTVKVEINE ETGQHLVSGM
GELHLEIIAH RIKERGVDIK VSEPIVVYRE GVFGVCDDEV EGKSPNKHNK FYVTVEPVEE
EIVEAIEEGK FNPEEMSKKE LEETLMEYGM DRDDAKAVET VKGTNFFLDK TVGLQYLNEV
MELLIEGFEE AMEEGPLAKE PCRGVKVSLV DAEIHEDPVH RGPAQVIPAI KRAIYGGMLL
ADTHLLEPMQ YIYVTVPQDY MGAVTKEIQG RRGTIEEIQQ EGDTVIIKGK APVAEMFGFA
NDIRSATEGR AIWTTEHAGY ERVPEELEEQ IIREIRERKG LKPEPPKPED YIEDYGG
